Surface-induced self-assembly of peptides turns superhydrophobic surface of electrospun fibrous into superhydrophilic one

Current surface modification strategies for electrospun materials always require covalent conjugation technology, which is relatively inefficient and might damage the bioactivity and structure of peptides and proteins. Here we introduce the use of surface-induced self-assembly technology to modify e...

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Veröffentlicht in:Colloids and surfaces, B, Biointerfaces B, Biointerfaces, 2025-01, Vol.245, p.114350, Article 114350
Hauptverfasser: Sun, Xuan, Ren, Han, Cui, Yue-Chan, Liu, Qian, Li, Jie, Gao, Jie
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Sprache:eng
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Zusammenfassung:Current surface modification strategies for electrospun materials always require covalent conjugation technology, which is relatively inefficient and might damage the bioactivity and structure of peptides and proteins. Here we introduce the use of surface-induced self-assembly technology to modify electrospun materials, which is a simple but efficient noncovalent-based process. Results show that the peptide NapFFGRGD forms burr-like structures on the surface of PCL fibers, reducing the water contact angle of the fibers. Adjusting the peptide sequence and salt concentration affects the self-assembly and surface properties of modified PCL fibers. Additionally, we demonstrate the potential application of this surface modification technique for enhancing cellular responses in tissue engineering applications. The research provides valuable insights into the surface modification of PCL fibers and offers a new method for improving the biological compatibility of materials in tissue engineering. [Display omitted] •Discovery of a simple but efficient noncovalent-based technology to modify electrospun materials with peptides.•Self-assembling peptides form burr-like structures on the surface of PCL fibers, reducing their water contact angle.•Adjusting peptide sequence and salt concentration affects the self-assembly and surface properties of modified PCL fibers.
ISSN:0927-7765
1873-4367
1873-4367
DOI:10.1016/j.colsurfb.2024.114350